Cargando…
G-actin provides substrate-specificity to eukaryotic initiation factor 2α holophosphatases
Dephosphorylation of eukaryotic translation initiation factor 2a (eIF2a) restores protein synthesis at the waning of stress responses and requires a PP1 catalytic subunit and a regulatory subunit, PPP1R15A/GADD34 or PPP1R15B/CReP. Surprisingly, PPP1R15-PP1 binary complexes reconstituted in vitro lac...
Autores principales: | Chen, Ruming, Rato, Cláudia, Yan, Yahui, Crespillo-Casado, Ana, Clarke, Hanna J, Harding, Heather P, Marciniak, Stefan J, Read, Randy J, Ron, David |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4394352/ https://www.ncbi.nlm.nih.gov/pubmed/25774600 http://dx.doi.org/10.7554/eLife.04871 |
Ejemplares similares
-
Actin dynamics tune the integrated stress response by regulating eukaryotic initiation factor 2α dephosphorylation
por: Chambers, Joseph E, et al.
Publicado: (2015) -
A Sephin1-insensitive tripartite holophosphatase dephosphorylates translation initiation factor 2α
por: Crespillo-Casado, Ana, et al.
Publicado: (2018) -
PPP1R15A-mediated dephosphorylation of eIF2α is unaffected by Sephin1 or Guanabenz
por: Crespillo-Casado, Ana, et al.
Publicado: (2017) -
AMPylation targets the rate-limiting step of BiP’s ATPase cycle for its functional inactivation
por: Preissler, Steffen, et al.
Publicado: (2017) -
Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker
por: Preissler, Steffen, et al.
Publicado: (2015)